CATL3_FASHE
ID CATL3_FASHE Reviewed; 19 AA.
AC P80532;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Putative cathepsin L3;
DE EC=3.4.22.15;
DE AltName: Full=Newly excysted juvenile protein 8;
DE Flags: Fragment;
OS Fasciola hepatica (Liver fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Fasciolidae;
OC Fasciola.
OX NCBI_TaxID=6192;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=7639732; DOI=10.1006/bbrc.1995.2112;
RA Tkalcevic J., Ashman K., Meeusen E.;
RT "Fasciola hepatica: rapid identification of newly excysted juvenile
RT proteins.";
RL Biochem. Biophys. Res. Commun. 213:169-174(1995).
CC -!- FUNCTION: Thiol protease.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specificity close to that of papain. As compared to cathepsin
CC B, cathepsin L exhibits higher activity toward protein substrates,
CC but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-
CC dipeptidase activity.; EC=3.4.22.15;
CC -!- SUBUNIT: Dimer of a heavy and a light chain linked by disulfide bonds.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the newly excysted juvenile stage.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR AlphaFoldDB; P80532; -.
DR BRENDA; 3.4.22.B62; 2230.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Lysosome; Protease;
KW Thiol protease.
FT CHAIN 1..>19
FT /note="Putative cathepsin L3"
FT /id="PRO_0000050540"
FT NON_TER 19
SQ SEQUENCE 19 AA; 2242 MW; 53FFB5835EBCB0D7 CRC64;
DVPASIDWRE YGYVTEVKD